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Proceedings Paper

Temperature Dependences Of The Infrared And Circular Dichroism Spectra Of Ribonuclease A And Troponin C
Author(s): Tatsuyuki Yamamoto; Masaru Tanokura; Mitsuo Tasumi
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Paper Abstract

Temperature dependences of the infrared and CD spectra of bovine pancreatic ribonuclease A and bullfrog skeletal muscle troponin C have been examined. In order to extract information on the secondary structure changes of these proteins from their infrared spectra, the methods of difference spectrum and Fourier-self-deconvolution have been applied. Both the infrared and circular dichroism spectra have confirmed that ribonuclease A undergoes thermal denaturation at 60°C in a typical manner. On the contrary, calcium-free troponin C shows gradual spectral changes with increasing temperature, indicating the absence of drastic conformational changes. No denaturation seems to take place for calcium-bound toponin C even at 80°C.

Paper Details

Date Published: 1 December 1989
PDF: 2 pages
Proc. SPIE 1145, 7th Intl Conf on Fourier Transform Spectroscopy, (1 December 1989); doi: 10.1117/12.969455
Show Author Affiliations
Tatsuyuki Yamamoto, The University of Tokyo (Japan)
Masaru Tanokura, Juntendo University School of Medicine (Japan)
Mitsuo Tasumi, The University of Tokyo (Japan)

Published in SPIE Proceedings Vol. 1145:
7th Intl Conf on Fourier Transform Spectroscopy
David G. Cameron, Editor(s)

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